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Database: UniProt
Entry: A0A166LHZ2_9AGAM
LinkDB: A0A166LHZ2_9AGAM
Original site: A0A166LHZ2_9AGAM 
ID   A0A166LHZ2_9AGAM        Unreviewed;       682 AA.
AC   A0A166LHZ2;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=PENSPDRAFT_747452 {ECO:0000313|EMBL:KZV76900.1};
OS   Peniophora sp. CONT.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Russulales; Peniophoraceae; Peniophora.
OX   NCBI_TaxID=1314672 {ECO:0000313|EMBL:KZV76900.1, ECO:0000313|Proteomes:UP000077086};
RN   [1] {ECO:0000313|EMBL:KZV76900.1, ECO:0000313|Proteomes:UP000077086}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CONT {ECO:0000313|EMBL:KZV76900.1,
RC   ECO:0000313|Proteomes:UP000077086};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KV424462; KZV76900.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A166LHZ2; -.
DR   STRING; 1314672.A0A166LHZ2; -.
DR   InParanoid; A0A166LHZ2; -.
DR   OrthoDB; 2052724at2759; -.
DR   Proteomes; UP000077086; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   PANTHER; PTHR32361:SF9; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 3-RELATED; 1.
DR   PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077086};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        201..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        269..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        303..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        332..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          353..507
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   682 AA;  72939 MW;  13E9AC0EF900513F CRC64;
     MSQYTFGLNP FVVVPAAGTY NNVPQVPVIV PSPARFGALP FVWHIDVLLC VLFGIFVLST
     LPRAVARYTA HGELFAGLYL RRGKPTNGAR GAAIATVPAA GHAMPKTPVP EAAMMMHDGA
     TVDDEGTMRL DAADAGLNEP AMPASSTTAS HAALLNYAVV DSDNGARQAV NPPAHISSYL
     ALTHPVISYV ANFPVAAGLP FKHFAVLLIY FGILLYVGVR GTSPFTDPRR PVDVAISQLP
     FVLAFSQKNN VLAVLSGLGY EKLNYLHRFV GRIIVLGVNL HTSYYLYRWS LDGTIYAQSR
     TSFVVWGIIG TAAVDVLFLL STAYVRARAY GLFLASHIFL SGLFVVAMYI HEPVTLPYFV
     TAFVLYGADH IFRAMRTRIV TVDLTAAPLL NGGSTIVSAP SLTTGWRAGQ HVRMRIIPAR
     GPRWLAVSWT WFAARFRARP FTISTRPGSS RGLELIVKKE GRSTQALFAR ATKDCPGSDG
     DPEKQCTGAC VKATVLLEGP YSGPGHALPQ AFSGALLLAG GSGITHALAL LDALAEAHAN
     GRSSCRVVDL VWATPDIASC VPLLPRFREL LAPRPSPHGS FMVRVSIHYT RVSSGAMKAL
     NPAELPAGLV LHAGRPYVRT VLADACRATA AAHPGVRPRG LVVSTCGPAQ ISEQAHAAVG
     SIAWDHWREV GGIEIVSETF GM
//
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